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Literature summary for 1.1.5.5 extracted from

  • Gvozdev, A.; Tukhvatullin, I.; Gvozdev, R.
    Quinone-dependent alcohol dehydrogenases and FAD-dependent alcohol oxidases (2012), Biochemistry, 77, 843-856.
    View publication on PubMed
Search for more literature for 1.1.5.5

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required, two ions, one bound in the active site, and one away from the active site near the N-terminus of the molecule. Dimensions of the active site cavity are provided by the stabilization of the spatial enzyme structure by the second Ca2+ ion Pseudomonas sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ethanol + ubiquinone Pseudomonas sp.
-
 acetaldehyde + ubiquinol
-
 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ethanol + ubiquinone
-
 Pseudomonas sp. acetaldehyde + ubiquinol
-
 ?

Subunits

Subunits Comment Organism
homodimer two alpha-subunits Pseudomonas sp.
More the enzyme shows a propeller structure, QEDH contains a disulfide structure that is similar to the analogous structure in QMDH, EC 1.1.2.8 Pseudomonas sp.

Synonyms

Synonyms Comment Organism
PQQ-dependent ethanol dehydrogenase
-
 Pseudomonas sp.
quinone-dependent alcohol dehydrogenase
-
 Pseudomonas sp.

Cofactor

Cofactor Comment Organism Structure
pyrroloquinoline quinone i.e. PQQ or 4,5-dihydro-4,5-dioxo-1H-pyrrolo[2,3f]quinoline-2,7,9-tricarboxylic acid Pseudomonas sp.